Evidence map›Paper›PMID 11294915›Full record

ArticleMolecular biology of the cell2001

Cadherin sequences that inhibit beta-catenin signaling: a study in yeast and mammalian cells.

I Simcha, C Kirkpatrick, E Sadot, M Shtutman, G Polevoy, B Geiger, M Peifer, A Ben-Ze'ev

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Nuclear signaling from cadherin adhesion complexes.Current topics in developmental biology · 2015
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Signaling from the adherens junction.Sub-cellular biochemistry · 2012
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

I SimchaDepartment of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel, 76100.
C Kirkpatrick
E Sadot
M Shtutman
G Polevoy
B Geiger
M Peifer
A Ben-Ze'ev
Weizmann Institute of Science · ILInstitut thématique Génétique, génomique et bioinformatique · FRUniversity of North Carolina at Chapel Hill · US

Funding

NRSA IN GENETICST32GM007092 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SEKELSKY, JEFF J. · 1985 to 2019
$5.9M
NIGMS NIH HHS 5T32 GM07092NIGMS NIH HHS T32 GM007092
6 · The paper itself

Abstract

Drosophila Armadillo and its mammalian homologue beta-catenin are scaffolding proteins involved in the assembly of multiprotein complexes with diverse biological roles. They mediate adherens junction assembly, thus determining tissue architecture, and also transduce Wnt/Wingless intercellular signals, which regulate embryonic cell fates and, if inappropriately activated, contribute to tumorigenesis. To learn more about Armadillo/beta-catenin's scaffolding function, we examined in detail its interaction with one of its protein targets, cadherin. We utilized two assay systems: the yeast two-hybrid system to study cadherin binding in the absence of Armadillo/beta-catenin's other protein partners, and mammalian cells where interactions were assessed in their presence. We found that segments of the cadherin cytoplasmic tail as small as 23 amino acids bind Armadillo or beta-catenin in yeast, whereas a slightly longer region is required for binding in mammalian cells. We used mutagenesis to identify critical amino acids required for cadherin interaction with Armadillo/beta-catenin. Expression of such short cadherin sequences in mammalian cells did not affect adherens junctions but effectively inhibited beta-catenin-mediated signaling. This suggests that the interaction between beta-catenin and T cell factor family transcription factors is a sensitive target for disruption, making the use of analogues of these cadherin derivatives a potentially useful means to suppress tumor progression.

Indexed as

Drosophila ProteinsTrans-ActivatorsAmino Acid SequenceAnimalsArmadillo Domain Proteinsbeta CateninBinding SitesCadherinsCell LineCell Line, TransformedCHO CellsCricetinaeCytoskeletal ProteinsDogsDrosophilaHumansArmadillo Domain ProteinsARM protein, Drosophilabeta CateninCadherinsCTNNB1 protein, humanCTNNB1 protein, mouseCytoskeletal ProteinsDrosophila ProteinsInsect ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID11294915
PMCPMC32295
OpenAlexW2079882222

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.